ArticleBiochemistry2014
Structure of human PIR1, an atypical dual-specificity phosphatase.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- DUSP11 is an Intracellular Innate Immune Checkpoint in Lung Adenocarcinoma.Cancer immunology research · 2025Article
- Structural analysis of dual specificity phosphatases, the only type of protein tyrosine phosphatases found in humans and across diverse microorganisms.Journal of microbiology (Seoul, Korea) · 2025Review
- Viral piracy of host RNA phosphatase DUSP11 by avipoxviruses.PLoS pathogens · 2025Article
- A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop.Nature communications · 2022Article
- The RNA phosphatase PIR-1 regulates endogenous small RNA pathways in C. elegans.Molecular cell · 2021Article
- DUSP11 and triphosphate RNA balance during virus infection.PLoS pathogens · 2021Article
- Review
- Molecular Architecture of the Inositol Phosphatase Siw14.Biochemistry · 2019Article
- Structural and biochemical characterization of Siw14: A protein-tyrosine phosphatase fold that metabolizes inositol pyrophosphates.The Journal of biological chemistry · 2018Article
- Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling.Nature communications · 2018Article
- DUSP11 - An RNA phosphatase that regulates host and viral non-coding RNAs in mammalian cells.RNA biology · 2017Article
- Structural basis for selective inhibition of Cyclooxygenase-1 (COX-1) by diarylisoxazoles mofezolac and 3-(5-chlorofuran-2-yl)-5-methyl-4-phenylisoxazole (P6).European journal of medicinal chemistry · 2017Article
- Crystal Structure of Hypothetical Fructose-Specific EIIB from Escherichia coli.Molecules and cells · 2016Article
- Dimeric quaternary structure of human laforin.The Journal of biological chemistry · 2015Article
- Genetically modified proteins: functional improvement and chimeragenesis.Bioengineered · 2015Review
- Voltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function research.Frontiers in pharmacology · 2015Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
PIR1 is an atypical dual-specificity phosphatase (DSP) that dephosphorylates RNA with a higher specificity than phosphoproteins. Here we report the atomic structure of a catalytically inactive mutant (C152S) of the human PIR1 phosphatase core (PIR1-core, residues 29-205), refined at 1.20 Å resolution. PIR1-core shares structural similarities with DSPs related to Vaccinia virus VH1 and with RNA 5'-phosphatases such as the baculovirus RNA triphosphatase and the human mRNA capping enzyme. The PIR1 active site cleft is wider and deeper than that of VH1 and contains two bound ions: a phosphate trapped above the catalytic cysteine C152 exemplifies the binding mode expected for the γ-phosphate of RNA, and ∼6 Å away, a chloride ion coordinates the general base R158. Two residues in the PIR1 phosphate-binding loop (P-loop), a histidine (H154) downstream of C152 and an asparagine (N157) preceding R158, make close contacts with the active site phosphate, and their nonaliphatic side chains are essential for phosphatase activity in vitro. These residues are conserved in all RNA 5'-phosphatases that, analogous to PIR1, lack a "general acid" residue. Thus, a deep active site crevice, two active site ions, and conserved P-loop residues stabilizing the γ-phosphate of RNA are defining features of atypical DSPs that specialize in dephosphorylating 5'-RNA.
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